p(HGNC:MAPT, pmod(Me, Lys, 290))

Entity

Name

MAPT

Namespace

hgnc

Namespace Version

20180906

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

Tau Modifications Sections of NESTOR

An example of a spectrum identifying K311 as a site of dimethylation at 2.2 ppm mass accuracy is shown in Fig. 2B. This residue was reported as a possible methylation site in AD-brain derived tau protein on the basis of Edman degradation years ago [36]. It resides within the “PHF6” motif of the MTBR, which has been reported to mediate the aggregation propensity of recombinant monomeric tau in vitro [6, 37]. Other methylation sites within the MTBR include K259, K290, and K353, each of which lies in a KXGS motif associated with AMP-activated protein kinase mediated regulation of microtubule binding [38]. Within the N-terminal projection domain, Lys methylation was detected at K24, K44, K67, and K190 (Fig. 1). PubMed:24869773

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876

An example of a spectrum identifying K311 as a site of dimethylation at 2.2 ppm mass accuracy is shown in Fig. 2B. This residue was reported as a possible methylation site in AD-brain derived tau protein on the basis of Edman degradation years ago [36]. It resides within the “PHF6” motif of the MTBR, which has been reported to mediate the aggregation propensity of recombinant monomeric tau in vitro [6, 37]. Other methylation sites within the MTBR include K259, K290, and K353, each of which lies in a KXGS motif associated with AMP-activated protein kinase mediated regulation of microtubule binding [38]. Within the N-terminal projection domain, Lys methylation was detected at K24, K44, K67, and K190 (Fig. 1). PubMed:24869773

However, robust monomethylation was identified at seven sites distributed throughout the tau sequence (Table 1). Three of the sites (K163, K174, and K180) reside within the proline-rich region of the tau N-terminal projection domain, which mediates interactions with microtubule-associated proteins such as actin [27] and the Src homology three domain of plasma membrane-associated proteins including Src family kinases [37] and phospholipase Cc [54]. In contrast, K254, K267, and K290 are part of the first and second repeats of the microtubule binding domain. Although no Lys acetylation was detected at these sites in our datasets, it was possible to quantify relative methylation and ubiquitylation of K254. PubMed:22033876